Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.
Identifieur interne : 001005 ( Main/Corpus ); précédent : 001004; suivant : 001006Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.
Auteurs : R. Bourbonnais ; M G PaiceSource :
- The Biochemical journal [ 0264-6021 ] ; 1988.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (isolation & purification), Alcohol Oxidoreductases (metabolism), Amino Acids (analysis), Basidiomycota (enzymology), Chromatography, Ion Exchange (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Kinetics (MeSH), Laccase (MeSH), Lignin (metabolism), Oxidoreductases (metabolism), Polyporaceae (enzymology), Spectrophotometry, Ultraviolet (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , isolation & purification : Alcohol Oxidoreductases.
- chemical , metabolism : Alcohol Oxidoreductases, Lignin, Oxidoreductases.
- enzymology : Basidiomycota, Polyporaceae.
- Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Kinetics, Laccase, Spectrophotometry, Ultraviolet, Substrate Specificity.
Abstract
The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.
DOI: 10.1042/bj2550445
PubMed: 3060110
PubMed Central: PMC1135248
Links to Exploration step
pubmed:3060110Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.</title><author><name sortKey="Bourbonnais, R" sort="Bourbonnais, R" uniqKey="Bourbonnais R" first="R" last="Bourbonnais">R. Bourbonnais</name><affiliation><nlm:affiliation>Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec.</nlm:affiliation></affiliation></author><author><name sortKey="Paice, M G" sort="Paice, M G" uniqKey="Paice M" first="M G" last="Paice">M G Paice</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1988">1988</date><idno type="RBID">pubmed:3060110</idno><idno type="pmid">3060110</idno><idno type="pmc">PMC1135248</idno><idno type="doi">10.1042/bj2550445</idno><idno type="wicri:Area/Main/Corpus">001005</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001005</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.</title><author><name sortKey="Bourbonnais, R" sort="Bourbonnais, R" uniqKey="Bourbonnais R" first="R" last="Bourbonnais">R. Bourbonnais</name><affiliation><nlm:affiliation>Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec.</nlm:affiliation></affiliation></author><author><name sortKey="Paice, M G" sort="Paice, M G" uniqKey="Paice M" first="M G" last="Paice">M G Paice</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1988" type="published">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (isolation & purification)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Amino Acids (analysis)</term><term>Basidiomycota (enzymology)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Kinetics (MeSH)</term><term>Laccase (MeSH)</term><term>Lignin (metabolism)</term><term>Oxidoreductases (metabolism)</term><term>Polyporaceae (enzymology)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amino Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Alcohol Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Lignin</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term><term>Polyporaceae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Ion Exchange</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Kinetics</term><term>Laccase</term><term>Spectrophotometry, Ultraviolet</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3060110</PMID><DateCompleted><Year>1989</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>255</Volume><Issue>2</Issue><PubDate><Year>1988</Year><Month>Oct</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.</ArticleTitle><Pagination><MedlinePgn>445-50</MedlinePgn></Pagination><Abstract><AbstractText>The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bourbonnais</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Paice</LastName><ForeName>M G</ForeName><Initials>MG</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C057990">veratryl alcohol oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002852" MajorTopicYN="N">Chromatography, Ion Exchange</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011124" MajorTopicYN="N">Polyporaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1988</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1988</Year><Month>10</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1988</Year><Month>10</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3060110</ArticleId><ArticleId IdType="pmc">PMC1135248</ArticleId><ArticleId IdType="doi">10.1042/bj2550445</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 1983 Aug 12;114(3):1077-83</Citation><ArticleIdList><ArticleId IdType="pubmed">6615503</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1983 Aug 12;221(4611):661-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17787736</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1985 Feb;49(2):299-304</Citation><ArticleIdList><ArticleId IdType="pubmed">16346716</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1987 May;169(5):2195-201</Citation><ArticleIdList><ArticleId IdType="pubmed">3553159</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1986 Aug;52(2):251-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16347125</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1969 Nov 25;244(22):6049-55</Citation><ArticleIdList><ArticleId IdType="pubmed">5389100</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1960 Feb;74:257-62</Citation><ArticleIdList><ArticleId IdType="pubmed">13821599</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1971 Oct 25;246(20):6339-46</Citation><ArticleIdList><ArticleId IdType="pubmed">4108384</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1976 May 7;72:248-54</Citation><ArticleIdList><ArticleId IdType="pubmed">942051</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1975 Jul;72(7):2515-9</Citation><ArticleIdList><ArticleId IdType="pubmed">1058470</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001005 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 001005 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= pubmed:3060110
|texte= Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:3060110" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |